GLR1/YPL091W Literature Guide Help

Other names published for GLR1: LPG17, glutathione-disulfide reductase GLR1, YPL091W

GLR1 - Substrates/Ligands/Cofactors (40)

ReferenceOther Genes Addressed
Rigobello MP, et al.  (2011) Interaction of selenite and tellurite with thiol-dependent redox enzymes: Kinetics and mitochondrial implications. Free Radic Biol Med 50(11):1620-9
Greetham D, et al.  (2010) Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae. BMC Biochem 11():3
Rousar T, et al.  (2010) Glutathione reductase is inhibited by acetaminophen-glutathione conjugate in vitro. Physiol Res 59(2):225-32
Seefeldt T, et al.  (2009) Characterization of a novel dithiocarbamate glutathione reductase inhibitor and its use as a tool to modulate intracellular glutathione. J Biol Chem 284(5):2729-37
Bayliak M, et al.  (2008) Inhibition of Catalase by Aminotriazole in vivo Results in Reduction of Glucose-6-phosphate Dehydrogenase Activity in Saccharomyces cerevisiae Cells. Biochemistry (Mosc) 73(4):420-6
Cardoso LA, et al.  (2008) Reductive inactivation of yeast glutathione reductase by Fe(II) and NADPH. Comp Biochem Physiol A Mol Integr Physiol 151(3):313-21
Galganska H, et al.  (2008) Redox regulation of protein expression in Saccharomyces cerevisiae mitochondria: Possible role of VDAC. Arch Biochem Biophys 479(1):39-45
Tandogan B and Ulusu NN  (2007) The inhibition kinetics of yeast glutathione reductase by some metal ions. J Enzyme Inhib Med Chem 22(4):489-95
Yu J and Zhou CZ  (2007) Crystal structure of glutathione reductase Glr1 from the yeast Saccharomyces cerevisiae. Proteins 68(4):972-9
Picaud T and Desbois A  (2006) Interaction of Glutathione Reductase with Heavy Metal: The Binding of Hg(II) or Cd(II) to the Reduced Enzyme Affects Both the Redox Dithiol Pair and the Flavin. Biochemistry 45(51):15829-15837
Trotter EW and Grant CM  (2005) Overlapping roles of the cytoplasmic and mitochondrial redox regulatory systems in the yeast Saccharomyces cerevisiae. Eukaryot Cell 4(2):392-400
Hou WC, et al.  (2004) Detection of glutathione reductase after electrophoresis on native or sodium dodecyl sulfate polyacrylamide gels. Electrophoresis 25(17):2926-31
Ostergaard H, et al.  (2004) Monitoring disulfide bond formation in the eukaryotic cytosol. J Cell Biol 166(3):337-45
Merwin JR, et al.  (2002) Reporter gene transactivation by human p53 is inhibited in thioredoxin reductase null yeast by a mechanism associated with thioredoxin oxidation and independent of changes in the redox state of glutathione. Carcinogenesis 23(10):1609-15
Picaud T and Desbois A  (2002) Electrostatic control of the isoalloxazine environment in the two-electron reduced states of yeast glutathione reductase. J Biol Chem 277(35):31715-21
Arscott LD, et al.  (2000) Mixed disulfide with glutathione as an intermediate in the reaction catalyzed by glutathione reductase from yeast and as a major form of the enzyme in the cell. Biochemistry 39(16):4711-21
Levron B, et al.  (2000) On the reduction of dithiolethiones and dithiolylium ions by NADPH and glutathione reductase. Arch Biochem Biophys 382(2):189-94
Baylor KJ and Heffron JJ  (1996) Isocyanate inactivation of yeast glutathione reductase & its modulation by oxidised glutathione and NADPH. Biochem Soc Trans 24(2):325S
Pick U, et al.  (1995) Glutathione reductase and lipoamide dehydrogenase have opposite stereospecificities for alpha-lipoic acid enantiomers. Biochem Biophys Res Commun 206(2):724-30
Alhama J, et al.  (1991) High-performance affinity chromatography of NADP+ dehydrogenases from cell-free extracts using a nucleotide analogue as general ligand. J Chromatogr 586(1):51-9
Cenas NK, et al.  (1991) Interaction of nitrofurans with glutathione reductase. Biochim Biophys Acta 1073(1):195-9
Cartana J, et al.  (1989) Characterization of the inhibition effect induced by nickel on glucose-6-phosphate dehydrogenase and glutathione reductase. Enzyme 41(1):1-5
Sahlman L and Williams CH Jr  (1989) Titration studies on the active sites of pig heart lipoamide dehydrogenase and yeast glutathione reductase as monitored by the charge transfer absorbance. J Biol Chem 264(14):8033-8
Llobell A, et al.  (1986) Electron transfer between reduced methyl viologen and oxidized glutathione: a new assay of Saccharomyces cerevisiae glutathione reductase. Arch Biochem Biophys 250(2):373-81
Huber PW and Brandt KG  (1985) Kinetic studies of the reduction of yeast glutathione reductase by reduced nicotinamide hypoxanthine dinucleotide phosphate. Arch Biochem Biophys 238(1):213-8
Pinto MC, et al.  (1985) The redox interconversion mechanism of Saccharomyces cerevisiae glutathione reductase. Eur J Biochem 151(2):275-81
Pinto MC, et al.  (1984) Reversible inactivation of Saccharomyces cerevisiae glutathione reductase under reducing conditions. Arch Biochem Biophys 228(1):1-12
Tsai CS  (1984) Recognition site of yeast glutathione reductase for 2'-phosphate of NADP+. Biochem Biophys Res Commun 124(2):572-7
Rafter GW  (1982) Copper inhibition of glutathione reductase and its reversal with gold thiolates, thiol, and disulfide compounds. Biochem Med 27(3):381-91
Dubler RE and Anderson BM  (1981) Simultaneous inactivation of the catalytic activities of yeast glutathione reductase by N-alkylmaleimides. Biochim Biophys Acta 659(1):70-85